AMRA1_HUMAN - dbPTM
AMRA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMRA1_HUMAN
UniProt AC Q9C0C7
Protein Name Activating molecule in BECN1-regulated autophagy protein 1
Gene Name AMBRA1
Organism Homo sapiens (Human).
Sequence Length 1298
Subcellular Localization Cytoplasmic vesicle, autophagosome. Localizes also to discrete punctae along the ciliary axoneme..
Protein Description Regulates autophagy and development of the nervous system. Involved in autophagy in controlling protein turnover during neuronal development, and in regulating normal cell survival and proliferation (By similarity)..
Protein Sequence MKVVPEKNAVRILWGRERGARAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQVGEQSTVQDSATPSPPPPPPQPSTERPRTSAYIRLRQRVSYPTAECCQHLGILCLCSRCSGTRVPSLLPHQDSVPPASARATTPSFSFVQTEPFHPPEQASSTQQDQGLLNRPSAFSTVQSSTAGNTLRNLSLGPTRRSLGGPLSSHPSRYHREIAPGLTGSEWTRTVLSLNSRSEAESMPPPRTSASSVSLLSVLRQQEGGSQASVYTSATEGRGFPASGLATESDGGNGSSQNNSGSIRHELQCDLRRFFLEYDRLQELDQSLSGEAPQTQQAQEMLNNNIESERPGPSHQPTPHSSENNSNLSRGHLNRCRACHNLLTFNNDTLRWERTTPNYSSGEASSSWQVPSSFESVPSSGSQLPPLERTEGQTPSSSRLELSSSASPQEERTVGVAFNQETGHWERIYTQSSRSGTVSQEALHQDMPEESSEEDSLRRRLLESSLISLSRYDGAGSREHPIYPDPARLSPAAYYAQRMIQYLSRRDSIRQRSMRYQQNRLRSSTSSSSSDNQGPSVEGTDLEFEDFEDNGDRSRHRAPRNARMSAPSLGRFVPRRFLLPEYLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVQNCKIYNDASCDISADGQLLAAFIPSSQRGFPDEGILAVYSLAPHNLGEMLYTKRFGPNAISVSLSPMGRYVMVGLASRRILLHPSTEHMVAQVFRLQQAHGGETSMRRVFNVLYPMPADQRRHVSINSARWLPEPGLGLAYGTNKGDLVICRPEALNSGVEYYWDQLNETVFTVHSNSRSSERPGTSRATWRTDRDMGLMNAIGLQPRNPATSVTSQGTQTLALQLQNAETQTEREVPEPGTAASGPGEGEGSEYGASGEDALSRIQRLMAEGGMTAVVQREQSTTMASMGGFGNNIIVSHRIHRSSQTGTEPGAAHTSSPQPSTSRGLLPEAGQLAERGLSPRTASWDQPGTPGREPTQPTLPSSSPVPIPVSLPSAEGPTLHCELTNNNHLLDGGSSRGDAAGPRGEPRNR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Ubiquitination------MKVVPEKNA
------CCCCCCHHH		64.34-
7Ubiquitination-MKVVPEKNAVRILW
-CCCCCCHHHHHHHH		44.10-
7 (in isoform 5)Ubiquitination-44.10-
36UbiquitinationLQELVEDKTRWMKWE
HHHHHHCCCCHHCCC		26.87-
36 (in isoform 5)Ubiquitination-26.87-
41UbiquitinationEDKTRWMKWEGKRVE
HCCCCHHCCCCEEEE		34.82-
41 (in isoform 5)Ubiquitination-34.82-
52PhosphorylationKRVELPDSPRSTFLL
EEEECCCCCCCEEEE		21.9221815630
83UbiquitinationNIYITEVKTGKCVHS
CEEEEEEECCCCHHH		45.38-
175UbiquitinationREPFAVVKTASEMER
CCCEEEEECHHHHCE		31.6021139048
175 (in isoform 1)Ubiquitination-31.6021890473
175 (in isoform 2)Ubiquitination-31.6021890473
175 (in isoform 3)Ubiquitination-31.6021890473
175 (in isoform 4)Ubiquitination-31.6021890473
175 (in isoform 5)Ubiquitination-31.6021890473
226DimethylationELSHYRQRALLQSQP
CCHHHHHHHHHHCCC		20.43-
269PhosphorylationVQDSATPSPPPPPPQ
CCCCCCCCCCCCCCC		45.7628985074
302MethylationSYPTAECCQHLGILC
CCCHHHHHHHHCHHH		1.83-
304PhosphorylationPTAECCQHLGILCLC
CHHHHHHHHCHHHHH		16.47-
304 (in isoform 5)Phosphorylation-16.4727251275
328PhosphorylationSLLPHQDSVPPASAR
CCCCCCCCCCCCCCC		29.9223186163
353PhosphorylationTEPFHPPEQASSTQQ
CCCCCCHHHCCCCHH		64.33-
375PhosphorylationPSAFSTVQSSTAGNT
CCHHHHHCCCCCCCC		31.58-
387PhosphorylationGNTLRNLSLGPTRRS
CCCCCCCCCCCCCCC		34.5311724133
391PhosphorylationRNLSLGPTRRSLGGP
CCCCCCCCCCCCCCC		36.6011724145
392MethylationNLSLGPTRRSLGGPL
CCCCCCCCCCCCCCC		29.35-
394PhosphorylationSLGPTRRSLGGPLSS
CCCCCCCCCCCCCCC		28.2428122231
400PhosphorylationRSLGGPLSSHPSRYH
CCCCCCCCCCCCHHC		29.7228122231
401PhosphorylationSLGGPLSSHPSRYHR
CCCCCCCCCCCHHCC		47.2928122231
404PhosphorylationGPLSSHPSRYHREIA
CCCCCCCCHHCCCCC		39.7927080861
406PhosphorylationLSSHPSRYHREIAPG
CCCCCCHHCCCCCCC		15.0127080861
415PhosphorylationREIAPGLTGSEWTRT
CCCCCCCCCCHHHHE		44.5729759185
417PhosphorylationIAPGLTGSEWTRTVL
CCCCCCCCHHHHEEE		25.4029759185
420PhosphorylationGLTGSEWTRTVLSLN
CCCCCHHHHEEECCC		16.6529759185
422O-linked_GlycosylationTGSEWTRTVLSLNSR
CCCHHHHEEECCCCC		20.5830059200
422PhosphorylationTGSEWTRTVLSLNSR
CCCHHHHEEECCCCC		20.5829759185
425PhosphorylationEWTRTVLSLNSRSEA
HHHHEEECCCCCCHH		22.5930631047
428PhosphorylationRTVLSLNSRSEAESM
HEEECCCCCCHHHCC		42.3428348404
430PhosphorylationVLSLNSRSEAESMPP
EECCCCCCHHHCCCC		40.7629759185
440O-linked_GlycosylationESMPPPRTSASSVSL
HCCCCCCCCHHHHHH		34.1230059200
441O-linked_GlycosylationSMPPPRTSASSVSLL
CCCCCCCCHHHHHHH		27.6830059200
441PhosphorylationSMPPPRTSASSVSLL
CCCCCCCCHHHHHHH		27.6823186163
443PhosphorylationPPPRTSASSVSLLSV
CCCCCCHHHHHHHHH		30.9223917254
449PhosphorylationASSVSLLSVLRQQEG
HHHHHHHHHHHHCCC		25.1324719451
465PhosphorylationSQASVYTSATEGRGF
CEEEEEEECCCCCCC		18.5911470115
545PhosphorylationIESERPGPSHQPTPH
CCCCCCCCCCCCCCC		31.18-
549PhosphorylationRPGPSHQPTPHSSEN
CCCCCCCCCCCCCCC		42.3419664995
549 (in isoform 4)Phosphorylation-42.3424719451
549 (in isoform 5)Phosphorylation-42.3427251275
603PhosphorylationASSSWQVPSSFESVP
CCCCCCCCCCCCCCC		14.7827251275
607 (in isoform 5)Phosphorylation-53.4222798277
612 (in isoform 5)Phosphorylation-36.0720068231
613 (in isoform 5)Phosphorylation-24.6120068231
626PhosphorylationLERTEGQTPSSSRLE
CCCCCCCCCCCCCEE		35.6726329039
628PhosphorylationRTEGQTPSSSRLELS
CCCCCCCCCCCEEEC		44.3115995481
629PhosphorylationTEGQTPSSSRLELSS
CCCCCCCCCCEEECC		22.2315995489
635PhosphorylationSSSRLELSSSASPQE
CCCCEEECCCCCCCH		16.9323401153
636PhosphorylationSSRLELSSSASPQEE
CCCEEECCCCCCCHH		42.4130266825
637PhosphorylationSRLELSSSASPQEER
CCEEECCCCCCCHHH		29.4130266825
639PhosphorylationLELSSSASPQEERTV
EEECCCCCCCHHHEE		29.1229255136
645PhosphorylationASPQEERTVGVAFNQ
CCCCHHHEEEEEEEC		25.5426074081
696PhosphorylationLRRRLLESSLISLSR
HHHHHHHHHHHHHHC		30.3446162843
697PhosphorylationRRRLLESSLISLSRY
HHHHHHHHHHHHHCC		21.9825003641
700PhosphorylationLLESSLISLSRYDGA
HHHHHHHHHHCCCCC		26.1124719451
704PhosphorylationSLISLSRYDGAGSRE
HHHHHHCCCCCCCCC		18.4918083107
707 (in isoform 4)Phosphorylation-15.1924719451
715PhosphorylationGSREHPIYPDPARLS
CCCCCCCCCCHHHCC		13.1618083107
722PhosphorylationYPDPARLSPAAYYAQ
CCCHHHCCHHHHHHH		13.6228555341
725PhosphorylationPARLSPAAYYAQRMI
HHHCCHHHHHHHHHH		10.97-
726PhosphorylationARLSPAAYYAQRMIQ
HHCCHHHHHHHHHHH		11.0518083107
730MethylationPAAYYAQRMIQYLSR
HHHHHHHHHHHHHHH		18.92-
733MethylationYYAQRMIQYLSRRDS
HHHHHHHHHHHHHHH		24.62-
747Asymmetric dimethylarginineSIRQRSMRYQQNRLR
HHHHHHHHHHHHHHH		27.62-
747MethylationSIRQRSMRYQQNRLR
HHHHHHHHHHHHHHH		27.62-
750MethylationQRSMRYQQNRLRSST
HHHHHHHHHHHHHCC		28.24-
754MethylationRYQQNRLRSSTSSSS
HHHHHHHHHCCCCCC		25.89-
757MethylationQNRLRSSTSSSSSDN
HHHHHHCCCCCCCCC		33.60-
762PhosphorylationSSTSSSSSDNQGPSV
HCCCCCCCCCCCCCC		42.3922210691
768PhosphorylationSSDNQGPSVEGTDLE
CCCCCCCCCCCCCCE		39.3622210691
786PhosphorylationFEDNGDRSRHRAPRN
CCCCCCCCCCCCCCC		36.8622210691
795MethylationHRAPRNARMSAPSLG
CCCCCCCCCCCHHHC		24.12-
797PhosphorylationAPRNARMSAPSLGRF
CCCCCCCCCHHHCCC		31.3223186163
798MethylationPRNARMSAPSLGRFV
CCCCCCCCHHHCCCC		6.59-
800PhosphorylationNARMSAPSLGRFVPR
CCCCCCHHHCCCCCH		43.0872840597
800 (in isoform 5)Phosphorylation-43.0827251275
803PhosphorylationMSAPSLGRFVPRRFL
CCCHHHCCCCCHHHC		34.38-
808MethylationLGRFVPRRFLLPEYL
HCCCCCHHHCCCHHH		22.09-
811MethylationFVPRRFLLPEYLPYA
CCCHHHCCCHHHCCC		2.52-
814PhosphorylationRRFLLPEYLPYAGIF
HHHCCCHHHCCCCCC		15.8417360941
817PhosphorylationLLPEYLPYAGIFHER
CCCHHHCCCCCCCCC		18.18-
824MethylationYAGIFHERGQPGLAT
CCCCCCCCCCCCCCC		40.24-
827MethylationIFHERGQPGLATHSS
CCCCCCCCCCCCCCC		42.46-
833PhosphorylationQPGLATHSSVNRVLA
CCCCCCCCCCHHHHC		31.4628555341
948PhosphorylationGPNAISVSLSPMGRY
CCCEEEEEECCCCCC		19.1529116813
955PhosphorylationSLSPMGRYVMVGLAS
EECCCCCCEEEEECC		6.2829116813
962PhosphorylationYVMVGLASRRILLHP
CEEEEECCCEEEECC		27.4329116813
1026PhosphorylationEPGLGLAYGTNKGDL
CCCCCEEECCCCCCE		29.538224415
1028PhosphorylationGLGLAYGTNKGDLVI
CCCEEECCCCCCEEE		22.5346162849
1046PhosphorylationEALNSGVEYYWDQLN
HHHHCCCCEEHHHHC		36.11-
1065PhosphorylationTVHSNSRSSERPGTS
EEECCCCCCCCCCCC		36.0529759185
1072PhosphorylationSSERPGTSRATWRTD
CCCCCCCCCCCCCCH		26.3229759185
1098PhosphorylationQPRNPATSVTSQGTQ
CCCCCCCCCCCCCCE		26.0428555341
1114 (in isoform 4)Phosphorylation-14.3024719451
1127O-linked_GlycosylationREVPEPGTAASGPGE
CCCCCCCCCCCCCCC		29.7530059200
1170PhosphorylationVVQREQSTTMASMGG
EEECHHHCCCCCCCC		21.9328555341
1191PhosphorylationVSHRIHRSSQTGTEP
EEEEEEECCCCCCCC		16.7928450419
1192PhosphorylationSHRIHRSSQTGTEPG
EEEEEECCCCCCCCC		31.5528450419
1194PhosphorylationRIHRSSQTGTEPGAA
EEEECCCCCCCCCCC		48.2828450419
1195PhosphorylationIHRSSQTGTEPGAAH
EEECCCCCCCCCCCC		22.05-
1196PhosphorylationHRSSQTGTEPGAAHT
EECCCCCCCCCCCCC		42.2528450419
1203PhosphorylationTEPGAAHTSSPQPST
CCCCCCCCCCCCCCC		26.6123911959
1204PhosphorylationEPGAAHTSSPQPSTS
CCCCCCCCCCCCCCC		30.1023911959
1205PhosphorylationPGAAHTSSPQPSTSR
CCCCCCCCCCCCCCC		28.8011214970
1206PhosphorylationGAAHTSSPQPSTSRG
CCCCCCCCCCCCCCC		50.2818691976
1207PhosphorylationAAHTSSPQPSTSRGL
CCCCCCCCCCCCCCC		46.6619664995
1207 (in isoform 5)Phosphorylation-46.6627251275
1208PhosphorylationAHTSSPQPSTSRGLL
CCCCCCCCCCCCCCC		42.8532645325
1209PhosphorylationHTSSPQPSTSRGLLP
CCCCCCCCCCCCCCH		33.4922115753
1210PhosphorylationTSSPQPSTSRGLLPE
CCCCCCCCCCCCCHH		29.1822115753
1211PhosphorylationSSPQPSTSRGLLPEA
CCCCCCCCCCCCHHH		28.7827794612
1227PhosphorylationQLAERGLSPRTASWD
HHHHCCCCCCCCCCC		18.3722199227
1230PhosphorylationERGLSPRTASWDQPG
HCCCCCCCCCCCCCC		28.5526074081
1238PhosphorylationASWDQPGTPGREPTQ
CCCCCCCCCCCCCCC		29.2950564911
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
52SPhosphorylationKinaseMTORP42345
PSP
465SPhosphorylationKinaseULK1O75385
PSP
635SPhosphorylationKinaseULK1O75385
PSP
1043SPhosphorylationKinaseIKKAO15111
PSP
-KUbiquitinationE3 ubiquitin ligaseRNF2Q99496
PMID:24980959
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMRA1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AMRA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB1_HUMANDDB1physical
20562859
MAP1B_HUMANMAP1Bphysical
20562859
ATG3_HUMANATG3physical
20562859
ATG4B_HUMANATG4Bphysical
20562859
DDA1_HUMANDDA1physical
20562859
PRKN_HUMANPARK2physical
21753002
BCL2_HUMANBCL2physical
21358617
ULK1_HUMANULK1physical
23524951
BECN1_HUMANBECN1physical
23974797
UB2D3_HUMANUBE2D3physical
23974797
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367
CUL4B_HUMANCUL4Bphysical
16949367
DYL1_HUMANDYNLL1physical
20921139
PK3C3_HUMANPIK3C3physical
20921139
GBRAP_HUMANGABARAPphysical
25215947
BECN1_HUMANBECN1physical
24587252
DDB1_HUMANDDB1physical
25499913
HS90A_HUMANHSP90AA1physical
25499913
GRP78_HUMANHSPA5physical
25499913
HSP7C_HUMANHSPA8physical
25499913
STIP1_HUMANSTIP1physical
25499913
TCPG_HUMANCCT3physical
25499913
CH60_HUMANHSPD1physical
25499913
TCPQ_HUMANCCT8physical
25499913
TCPD_HUMANCCT4physical
25499913
TCPB_HUMANCCT2physical
25499913
TBA1A_HUMANTUBA1Aphysical
25499913
TBB3_HUMANTUBB3physical
25499913
BAG5_HUMANBAG5physical
25499913
DNJB1_HUMANDNAJB1physical
25499913
ACTN1_HUMANACTN1physical
25499913
SGT1_HUMANSUGT1physical
25499913
CHIP_HUMANSTUB1physical
25499913
BAG2_HUMANBAG2physical
25499913
ELOB_HUMANTCEB2physical
25499913
CUL4A_HUMANCUL4Aphysical
25499913
CUL4B_HUMANCUL4Bphysical
25499913
WDR1_HUMANWDR1physical
25499913
DDA1_HUMANDDA1physical
25499913
CSN1_HUMANGPS1physical
25499913
CSN8_HUMANCOPS8physical
25499913
PSA1_HUMANPSMA1physical
25499913
PSA2_HUMANPSMA2physical
25499913
PSA3_HUMANPSMA3physical
25499913
PSA4_HUMANPSMA4physical
25499913
PSA5_HUMANPSMA5physical
25499913
PSA6_HUMANPSMA6physical
25499913
PSA7_HUMANPSMA7physical
25499913
PSB2_HUMANPSMB2physical
25499913
PSB3_HUMANPSMB3physical
25499913
PSB5_HUMANPSMB5physical
25499913
PRS4_HUMANPSMC1physical
25499913
PRS7_HUMANPSMC2physical
25499913
PRS6A_HUMANPSMC3physical
25499913
PRS6B_HUMANPSMC4physical
25499913
PRS8_HUMANPSMC5physical
25499913
PRS10_HUMANPSMC6physical
25499913
PSMD2_HUMANPSMD2physical
25499913
PSMD3_HUMANPSMD3physical
25499913
PSMD6_HUMANPSMD6physical
25499913
PSMD8_HUMANPSMD8physical
25499913
PSD10_HUMANPSMD10physical
25499913
PSD12_HUMANPSMD12physical
25499913
PSD13_HUMANPSMD13physical
25499913
UBL4A_HUMANUBL4Aphysical
25499913
UBC_HUMANUBCphysical
25499913
CUL7_HUMANCUL7physical
25499913
PP2AA_HUMANPPP2CAphysical
25438055
2AAA_HUMANPPP2R1Aphysical
25438055
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMRA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND MASSSPECTROMETRY.

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